Activator of G Protein Signaling 3 Null Mice: I. Unexpected Alterations in Metabolic and Cardiovascular Function

Blumer, Joe B.; Lord, Kevin; Saunders, Thomas L.; Pacchioni, Alejandra M.; Black, Cory; Lazartigues, Eric; Varner, Kurt J.; Gettys, Thomas W.; Lanier, Stephen M.

doi:10.1210/en.2008-0050

Cited by 59 publications

(58 citation statements)

References 54 publications

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“…Among those DEGs, ATP synthase subunits, NADH dehydrogenase, and Diablo homolog are linked to mitochondrial and cellular metabolism (Wathes et al 2012). Different signaling pathway molecules are also differentially expressed, such as Wnt-2b and b-catenin in regulating Wnt pathway (Mosimann et al 2009), MAPK and MAPKK in MAPK pathway (Raabe & Rapp 2002), and GPSM1 in G-protein signaling (Blumer et al 2008). In addition, proteins required for transport are also differentially expressed, such as Zinc transporter ZIP13, intraflagellar transport 122 homolog, long-chain fatty Genome-wide transcriptome analysis acid transport protein 1, and protein transport protein Sec61 subunits.…”

Section: Discussionmentioning

confidence: 99%

Genome-wide transcriptome analysis between Small-tail Han sheep and the Surabaya fur sheep using high-throughput RNA sequencing

Miao¹,

Luo²

2013

Reproduction

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The Small-tail Han sheep and the Surabaya fur sheep are two local breeds in North China, which are characterized by high-fecundity and low-prolificacy breed respectively. Significant genetic differences between these two breeds have provided increasing interests in the identification and utilization of major prolificacy genes in these sheep. High prolificacy is a complex trait, and it is difficult to comprehensively identify the candidate genes related to this trait using the single molecular biology technique. To understand the molecular mechanisms of fecundity and provide more information about high prolificacy candidate genes in high-and low-fecundity sheep, we explored the utility of next-generation sequencing technology in this work. A total of 1.8 Gb sequencing reads were obtained and resulted in more than 20 000 contigs that averaged w300 bp in length. Ten differentially expressed genes were further verified by quantitative real-time RT-PCR to confirm the reliability of RNA-seq results. Our work will provide a basis for the future research of the sheep reproduction.

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Section: Discussionmentioning

confidence: 99%

Genome-wide transcriptome analysis between Small-tail Han sheep and the Surabaya fur sheep using high-throughput RNA sequencing

Miao¹,

Luo²

2013

Reproduction

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“…Pins has two mammalian homologs, Ags3 and Lgn (G-protein regulator; Gpsm1 and Gpsm2 -Mouse Genome Informatics) (Yu et al, 2003;Sanada and Tsai, 2005). Ags3-null mice show no defects in brain morphology or function (Blumer et al, 2008). By contrast, knocking out Lgn randomizes the orientation of normally planar neuroepithelial divisions, consistent with it having a role in mitotic spindle orientation in the developing brain (Morin et al, 2007;Konno et al, 2008).…”

Section: Parallels To Mammalian Neural Stem Cellsmentioning

confidence: 93%

Drosophila neuroblasts: a model for stem cell biology

2012

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SummaryDrosophila neuroblasts, the stem cells of the developing fly brain, have emerged as a key model system for neural stem cell biology and have provided key insights into the mechanisms underlying asymmetric cell division and tumor formation. More recently, they have also been used to understand how neural progenitors can generate different neuronal subtypes over time, how their cell cycle entry and exit are coordinated with development, and how proliferation in the brain is spared from the growth restrictions that occur in other organs upon starvation. In this Primer, we describe the biology of Drosophila neuroblasts and highlight the most recent advances made using neuroblasts as a model system.

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“…LGN binding to the Mud-related protein nuclear mitotic apparatus protein (NuMA) via the TPR domain is also considered to participate in mitotic spindle orientation (7). In addition, a mutation in the human LGN gene has been identified as cause for nonsyndromic deafness (17); ablation of AGS3 in mice leads to alterations in metabolic function (18) and impaired renal tubular regeneration after acute kidney injury (19). The mammalian Pinsrelated proteins thus contribute to a variety of biological events.…”

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confidence: 99%

Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)

Yuzawa

Kamakura

Iwakiri

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Interaction between the mammalian cell polarity proteins mInsc (mammalian homologue of Inscuteable) and Leu-Gly-Asn repeatenriched protein (LGN), as well as that between their respective Drosophila homologues Inscuteable and Partner of Inscuteable (Pins), plays crucial roles in mitotic spindle orientation, a process contributing to asymmetric cell division. Here, we report a crystal structure of the LGN-binding domain (LBD) of human mInsc complexed with the N-terminal tetratricopeptide repeat (TPR) motifs of human LGN at 2.6-Å resolution. In the complex, mInsc-LBD adopts an elongated structure with three binding modules-an α-helix, an extended region, and a β-sheet connected with a loop-that runs antiparallel to LGN along the concave surface of the superhelix formed by the TPRs. Structural analysis and structure-based mutagenesis define residues that are critical for mInsc-LGN association, and reveal that the activator of G-protein signaling 3 (AGS3)-binding protein Frmpd1 [4.1/ezrin/radixin/moesin (FERM) and PSD-95/Dlg/ZO-1 (PDZ) domain-containing protein 1] and its relative Frmpd4 interact with LGN via a region homologous to a part of mInsc-LBD, whereas nuclear mitotic apparatus protein (NuMA) and the C terminus of LGN recognize the TPR domain in a manner different from that by mInsc. mInsc binds to LGN with the highest affinity (K D ≈ 2.4 nM) and effectively replaces the Frmpd proteins, NuMA, and the LGN C terminus, suggesting the priority of mInsc in binding to LGN. We also demonstrate, using mutant proteins, that mInsc-LGN interaction is vital for stabilization of LGN and for intracellular localization of mInsc. C ell polarization plays an essential role in asymmetric cell division, cell migration, and the proper function of various differentiated cell types (1). In the fruit fly Drosophila melanogaster, neurons and glial cells are produced by asymmetric division of neuroblasts that delaminate as single cells from apical-basal polarized neuroectoderm (2). The asymmetric division requires establishment of apical-basal polarity in neuroblasts; the Bazookacontaining protein complex is specifically localized to the apical cortex for polarity establishment. The mitotic spindle poles, normally arranged in parallel to the plane of the neuroectoderm, are also needed to be oriented along the apical-basal axis, which orientation is driven by another evolutionarily conserved protein complex containing Partner of Inscuteable (Pins), Mud, and the Gαi subunit of trimeric Gi proteins. The adaptor protein Inscuteable (Insc) simultaneously binds to Bazooka and Pins to provide a physical link between the two complexes; the link thereby couples cortical cell polarity and spindle orientation for asymmetric cell division.Homologues of both Insc and Pins are known to exist exclusively in animals (from insects to mammals). The mammalian homologue of Insc (mInsc) also appears to contribute to mitotic spindle orientation and asymmetric cell division. Like Drosophila Insc, mInsc is capable of simultaneously interacting with the mamm...

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Activator of G Protein Signaling 3 Null Mice: I. Unexpected Alterations in Metabolic and Cardiovascular Function

Cited by 59 publications

References 54 publications

Genome-wide transcriptome analysis between Small-tail Han sheep and the Surabaya fur sheep using high-throughput RNA sequencing

Genome-wide transcriptome analysis between Small-tail Han sheep and the Surabaya fur sheep using high-throughput RNA sequencing

Drosophila neuroblasts: a model for stem cell biology

Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)

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